ID N6W6B6_9ACTO Unreviewed; 902 AA.
AC N6W6B6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN Name=ppsA {ECO:0000313|EMBL:ENO18065.1};
GN ORFNames=HMPREF9004_1190 {ECO:0000313|EMBL:ENO18065.1};
OS Schaalia cardiffensis F0333.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO18065.1, ECO:0000313|Proteomes:UP000013015};
RN [1] {ECO:0000313|EMBL:ENO18065.1, ECO:0000313|Proteomes:UP000013015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0333 {ECO:0000313|EMBL:ENO18065.1,
RC ECO:0000313|Proteomes:UP000013015};
RA Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT "Reference genome for the Human Microbiome Project.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENO18065.1}.
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DR EMBL; AQHZ01000020; ENO18065.1; -; Genomic_DNA.
DR RefSeq; WP_005963340.1; NZ_KB822674.1.
DR AlphaFoldDB; N6W6B6; -.
DR STRING; 888050.HMPREF9004_1190; -.
DR PATRIC; fig|888050.3.peg.1131; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_11; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000013015; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.80.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 2.
DR PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:ENO18065.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ENO18065.1}.
FT DOMAIN 53..285
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 293..350
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 420..484
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 544..893
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 451
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 857
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 581
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 637
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 770
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 791
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 792
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 793
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 902 AA; 97962 MW; FB9342BCBD5B9546 CRC64;
MVKYVYDFSE GDKSMKDLLG GKGANLAEMT KLGLPVPPGF TITTEACRAY LKDSLVPESL
ATEVTAALRG VEDQMERTLG DPDNPLLVSV RSGAKFSMPG MMETVLNIGL NDQSVLGLAK
ISGNERFAWD SYRRLIQMFG KTVLDIDGDL FSDALDSLKA ERGVTGDTEL TAEDLKGLVV
TFKKIVSEQK GMDFPQDPRA QMDMAIEAVF RSWNTERARI YRRRERIPHD LGTAVNICTM
VFGNMGEGSG TGVCFTRDPS SGHSGVYGDY LENAQGEDVV AGIRNTLSLA DLEDIDKASY
DKLRGIMRKL ETHYRDMCDI EFTIERGKLW MLQTRVGKRT AAAAFRIAIQ LVEEKLITRD
EALARVTGDQ LTQLMFPQFD QKASKEFVAR GMAASPGAAV GKIAFDNAQA EAFSAKGVKC
VLVRRETNPD DLPGMVVAEG VLTARGGKTS HAAVVARGMG KTCVCGAEAL EINAEARTVT
IDGRVFTSDD TIAIDGQTGE IFSGDVPVTD SPVTTYLAEG LEAGLAAAGA DEGTRELVKA
VDFILTHADK VRRLRVRANA DTPADSRRSI EFGAEGIGLC RTEHMFLGSR RPLVERAILS
APGSDERTAA FAELEKLQRQ DFLEMLEVMD GKSMTVRLID PPLHEFMPAL SELEIKVAVA
KATGEVDPAD ERMLMEVRRF HEQNPMLGLR GVRLGIYLPG LFALQMRALC EAAADLVAKG
LDPKPEIMVP LVGSVRELQL IREEGEAIIA EVQEARGVNL SGVTIGAMIE LPRAAMTAED
LAEEADFFSF GTNDLTQTVW GFSRDDVEGV FFPQYLEAGI FGVSPFESID VHGVGTLVRE
GVTRARSTKP GIKLGVCGEH GGDPASIHFF HEVGVDYVSC SPFRVPVARL EAGRAAVLTE
ES
//
